Mammalian septins constitute a family of at least 12 GTP-binding proteins that can form
hetero-oligomers and that are sometimes found in association with actin or microtubule …

The actin and microtubule cytoskeletons comprise a variety of networks with distinct
architectures, dynamics and protein composition. A fundamental question in eukaryotic cell …

Cellular morphogenesis and processes such as cell division and migration require the
coordination of the microtubule and actin cytoskeletons. Microtubule–actin crosstalk is …

Septins are GTP‐binding proteins that associate with the microtubule (MT) and actin
cytoskeleton. Septins affect MT organization and posttranslational modifications, but their …

Septins comprise an evolutionarily conserved family of oligomeric GTPases that regulate the
intracellular localization of proteins by functioning as protein scaffolds and diffusion barriers …

Septin GTP-binding proteins contribute essential biological functions that range from the
establishment of cell polarity to animal tissue morphogenesis. Human septins in cells form …

Septins are members of a conserved family of cytoskeletal GTPases present in organisms as
diverse as yeast and mammals. Unlike lower eukaryotic cells, the physiological significance …

Septins are a family of conserved proteins implicated in a variety of cellular functions such
as cytokinesis and vesicle trafficking, but their properties and modes of action are largely …

Septins are a family of conserved proteins that have been implicated in a variety of cellular
functions involving specialized regions of the cell cortex and changes in cell shape. The …

Septins (SEPTs) are filamentous guanosine-5′-triphosphate (GTP)-binding proteins, which
affect microtubule (MT)-dependent functions including membrane trafficking and cell …